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7LPR
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BU of 7lpr by Molmil
STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Fujishige, A, Bone, R, Agard, D.A.
Deposit date:1991-08-05
Release date:1993-01-15
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Structural basis for broad specificity in alpha-lytic protease mutants.
Biochemistry, 30, 1991
3LPR
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BU of 3lpr by Molmil
STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-NORLEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Bone, R, Agard, D.A.
Deposit date:1991-08-05
Release date:1993-01-15
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Structural basis for broad specificity in alpha-lytic protease mutants.
Biochemistry, 30, 1991
2ZCI
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BU of 2zci by Molmil
Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum
Descriptor: Phosphoenolpyruvate carboxykinase [GTP]
Authors:Aich, S, Prasad, L, Delbaere, L.T.J.
Deposit date:2007-11-09
Release date:2008-04-15
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum.
Int.J.Biochem.Cell Biol., 40, 2008
3CCD
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BU of 3ccd by Molmil
1.0 A Structure of Post-Succinimide His15Asp HPr
Descriptor: Phosphocarrier protein HPr, SULFATE ION
Authors:Napper, S, Prasad, L, Delbaere, L.T.J.
Deposit date:2008-02-25
Release date:2008-10-21
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (1 Å)
Cite:Structural investigation of a phosphorylation-catalyzed, isoaspartate-free, protein succinimide: crystallographic structure of post-succinimide His15Asp histidine-containing protein
Biochemistry, 47, 2008
1AQ2
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BU of 1aq2 by Molmil
PHOSPHOENOLPYRUVATE CARBOXYKINASE
Descriptor: ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, MANGANESE (II) ION, ...
Authors:Tari, L.W, Matte, A, Goldie, H, Delbaere, L.T.J.
Deposit date:1997-08-05
Release date:1998-10-14
Last modified:2023-11-15
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions.
Nat.Struct.Biol., 4, 1997
1K3D
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BU of 1k3d by Molmil
Phosphoenolpyruvate carboxykinase in complex with ADP and AlF3
Descriptor: ADENOSINE-5'-DIPHOSPHATE, ALUMINUM FLUORIDE, MAGNESIUM ION, ...
Authors:Sudom, A.M, Prasad, L, Goldie, H, Delbaere, L.T.J.
Deposit date:2001-10-02
Release date:2001-12-19
Last modified:2023-08-16
Method:X-RAY DIFFRACTION (2 Å)
Cite:The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3).
J.Mol.Biol., 314, 2001
1K3C
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BU of 1k3c by Molmil
Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate
Descriptor: ADENOSINE-5'-DIPHOSPHATE, ALUMINUM FLUORIDE, MAGNESIUM ION, ...
Authors:Sudom, A.M, Prasad, L, Goldie, H, Delbaere, L.T.J.
Deposit date:2001-10-02
Release date:2001-12-19
Last modified:2023-11-15
Method:X-RAY DIFFRACTION (2 Å)
Cite:The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3).
J.Mol.Biol., 314, 2001
1AYL
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BU of 1ayl by Molmil
PHOSPHOENOLPYRUVATE CARBOXYKINASE
Descriptor: ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, OXALATE ION, ...
Authors:Tari, L.W, Pugazenthi, U, Goldie, H, Delbaere, L.T.J.
Deposit date:1995-12-07
Release date:1997-01-11
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase.
Nat.Struct.Biol., 3, 1996
2LPR
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BU of 2lpr by Molmil
STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-VALINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Bone, R, Agard, D.A.
Deposit date:1991-08-05
Release date:1993-01-15
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Structural basis for broad specificity in alpha-lytic protease mutants.
Biochemistry, 30, 1991
1FU0
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BU of 1fu0 by Molmil
CRYSTAL STRUCTURE ANALYSIS OF THE PHOSPHO-SERINE 46 HPR FROM ENTEROCOCCUS FAECALIS
Descriptor: PHOSPHOCARRIER PROTEIN HPR
Authors:Audette, G.F, Engelmann, R, Hengstenberg, W, Deutscher, J, Hayakawa, K, Quail, J.W, Delbaere, L.T.J.
Deposit date:2000-09-13
Release date:2000-11-22
Last modified:2022-12-21
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis.
J.Mol.Biol., 303, 2000
1FX5
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BU of 1fx5 by Molmil
CRYSTAL STRUCTURE ANALYSIS OF ULEX EUROPAEUS LECTIN I
Descriptor: (4R)-2-METHYLPENTANE-2,4-DIOL, ANTI-H(O) LECTIN I, CALCIUM ION, ...
Authors:Audette, G.F, Vandonselaar, M, Delbaere, L.T.J.
Deposit date:2000-09-25
Release date:2001-01-17
Last modified:2023-08-09
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:The 2.2 A resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus.
J.Mol.Biol., 304, 2000
1GBD
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BU of 1gbd by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBF
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BU of 1gbf by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBL
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BU of 1gbl by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBI
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BU of 1gbi by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBJ
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BU of 1gbj by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA
Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBC
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BU of 1gbc by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBE
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BU of 1gbe by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU
Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBH
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BU of 1gbh by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBK
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BU of 1gbk by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.13 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBM
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BU of 1gbm by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.28 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBA
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BU of 1gba by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA
Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBB
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BU of 1gbb by Molmil
Alpha-lytic protease with met 190 replaced by ALA AND GLY 216 replaced by ALA complex with METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1CM2
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BU of 1cm2 by Molmil
STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.
Descriptor: HISTIDINE-CONTAINING PROTEIN
Authors:Napper, S, Delbaere, L.T.J, Waygood, E.B.
Deposit date:1999-05-13
Release date:2000-05-17
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization
J.Biol.Chem., 274, 1999
1CM3
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BU of 1cm3 by Molmil
HIS15ASP HPR FROM E. COLI
Descriptor: HISTIDINE-CONTAINING PROTEIN
Authors:Napper, S, Waygood, E.B, Delbaere, L.T.J.
Deposit date:1999-05-13
Release date:2000-05-17
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization
J.Biol.Chem., 274, 1999

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數據於2024-09-25公開中

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